Any feedback?
Information on EC 1.13.12.2 - lysine 2-monooxygenase
for references in articles please use BRENDA:EC1.13.12.2Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.13.12.2 lysine 2-monooxygenaseIUBMB Comments
A flavoprotein (FAD). Also acts on other diamino acids.
Specify your search results
Word Map
- 1.13.12.2
- putida
- 5-aminovalerate
- glutarate
-
fed-batch
-
nylon
- synthesis
- fluorescens
- semialdehyde
- 1,5-pentanediol
- polyamides
- glutamicum
- flavoproteins
-
corynebacterium
- l-pipecolate
- biotechnology
- 4-aminobutyrate
-
five-carbon
-
amidohydrolase
-
his6-tagged
- cadaverine
- biomass
- transaminase
-
permease
-
byproduct
-
deamination
- putrescine
-
bio-based
-
feedstock
-
codon-optimized
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
lysine 2-monooxygenase, l-amino acid oxidase/monooxygenase, l-lysine monooxygenase, l-lysine-2-monooxygenase, l-lysine 2-monooxygenase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
davB
L-LOX/MOG
L-lysine 2-monooxygenase
L-lysine oxidase/monooxygenase
L-lysine-2-monooxygenase
-
-
-
-
lysine monooxygenase
lysine oxygenase
-
-
-
-
lysine monooxygenase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-lysine + O2 = 5-aminopentanamide + CO2 + H2O
a slight difference of the binding position of a substrate dictates the activity of this type of enzyme as oxidase or monooxygenase, residue C254 is involved
L-lysine + O2 = 5-aminopentanamide + CO2 + H2O
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-lysine:oxygen 2-oxidoreductase (decarboxylating)
A flavoprotein (FAD). Also acts on other diamino acids.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9031-22-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-methyllysine + O2
2-keto-4-methyl-6-amino-n-hexanoate + NH3 + H2O2
-
oxidase activity
-
?
5-methyllysine + O2
4-methyl-5-aminopentanamide + CO2 + H2O
-
monooxygenase activity
-
?
alanine + propylamine + O2
?
-
monooxygenase and oxidase activity
-
-
?
alanine + propylamine + phenazine methosulfate
pyruvate + NH3 + reduced phenazine methosulfate
-
anaerobic conditions, ferricyanide as terminal electron acceptor, dehydrogenase activity
-
?
DL-2,8-diaminooctanoate + O2
2-keto-8-aminooctanoate + NH3 + H2O2
-
oxidase activity
-
-
?
DL-7,8-diaminoheptanoate + O2
6-aminohexanamide + CO2 + H2O
-
monooxygenase activity
-
-
?
L-arginine + O2
2-amino-5-guanidinovalerate + NH3 + H2O2
-
oxidase activity
-
-
?
L-arginine + O2
4-guanidinobutanamide + CO2 + H2O
-
-
-
?
L-arginine + phenazine methosulfate
2-keto-5-guanidinovalerate + NH3 + reduced phenazine methosulfate
-
anaerobic conditions, ferricyanide as terminal electron acceptor, dehydrogenase activity
-
?
L-lysine + electron acceptor
?
-
anaerobic conditions, electron acceptors are methylene blue, toluylene blue, phenol blue or thymol indophenol
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
enzymes with dual activities in a single active site: L-lysine oxidase and L-lysine monooxygenase
-
-
?
L-lysine + phenazine methosulfate
2-keto-6-amino-n-hexanoate + NH3 + reduced phenazine methosulfate
-
anaerobic conditions, ferricyanide as terminal electron acceptor, dehydrogenase activity
-
?
L-ornithine + O2
2-keto-5-amino-n-pentanoate + NH3 + H2O2
-
oxidase activity
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoate + NH3 + H2O2
-
enzymes with dual activities in a single active site: L-lysine oxidase and L-lysine monooxygenase
-
-
?
L-ornithine + phenazine methosulfate
2-keto-5-aminopentanoate + NH3 + reduced phenazine methosulfate
-
anaerobic conditions, ferricyanide as terminal electron acceptor, dehydrogenase activity
-
?
Nepsilon-methyllysine + O2
5-methylaminopentanamide + CO2 + H2O
-
monooxygenase activity
-
?
L-arginine + O2
4-guanidinobutyramide + CO2 + H2O
-
monooxygenase activity
-
-
?
L-arginine + O2
4-guanidinobutyramide + CO2 + H2O
-
monooxygenase activity
-
?
L-arginine + O2
4-guanidinobutyramide + CO2 + H2O
-
monooxygenase activity
-
-
?
L-lysine + O2
2-keto-6-amino-n-hexanoate + NH3 + H2O2
-
oxidase activity
-
?
L-lysine + O2
2-keto-6-amino-n-hexanoate + NH3 + H2O2
-
oxidase activity
-
-
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
monooxygenase activity
-
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
monooxygenase activity
-
-
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
monooxygenase activity
-
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
monooxygenase activity
-
-
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
monooxygenase activity
-
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
-
-
-
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
-
-
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
the mechanistic features are reported that are important for allowing the single active site of L-LOX/MOG to catalyze the two reactions of apparent monooxygenation and the oxidation of the flavoprotein oxidase
-
-
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
preferred substrate
-
-
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
enzymes with dual activities in a single active site: L-lysine oxidase and L-lysine monooxygenase
-
-
?
L-ornithine + O2
4-aminobutanamide + CO2 + H2O
-
enzymes with dual activities in a single active site: L-lysine oxidase and L-lysine monooxygenase
-
-
?
additional information
?
-
-
analogs with a modified carboxyl or alpha-amino group are inactive as substrates
-
-
?
additional information
?
-
-
monooxygenase, oxidase and dehydrogenase reaction catalyzed by a single enzyme molecule
-
-
?
additional information
?
-
-
monooxygenase, oxidase and dehydrogenase reaction catalyzed by a single enzyme molecule
-
-
?
additional information
?
-
-
enzyme specific for O2 as electron acceptor, no dehydrogenase activity
-
-
?
additional information
?
-
-
alkylamine dependent oxygenation of alpha-monoamino acids
-
-
?
additional information
?
-
-
alkylamine dependent oxygenation of alpha-monoamino acids
-
-
?
additional information
?
-
-
L-lysine analogs with a chloro or hydroxyl group at either the delta or the gamma position are both oxygenated and oxidized
-
-
?
additional information
?
-
bifunctional L-amino acid oxidase, EC 1.4.3.2, of Pseudomonas sp. AIU813, renamed as L-amino acid oxidase/monooxygenase (L-AAO/MOG), exhibits L-lysine 2-monooxygenase as well as oxidase activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
bifunctional L-amino acid oxidase, EC 1.4.3.2, of Pseudomonas sp. AIU813, renamed as L-amino acid oxidase/monooxygenase (L-AAO/MOG), exhibits L-lysine 2-monooxygenase as well as oxidase activity
-
-
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
-
-
-
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-Methyllysine
-
at higher substrate concentrations, competitive inhibitor
5-Methyllysine
-
at higher substrate concentrations, competitive inhibitor
alkylamines
-
high concentration inhibits, low concentrations stimulate lysine oxygenation
Nepsilon-Methyllysine
-
at higher substrate concentrations, competitive inhibitor
ornithine
-
at low concentration of L-lysine reaction is stimulated by L-ornithine, at high concentrations of L-lysine it is inhibited
p-chloromercuribenzoate
-
increases oxidase and dehydrogenase activities, decreases oxygenase activity
p-chloromercuribenzoate
-
conversion of oxygenase to oxidase; increases oxidase and dehydrogenase activities, decreases oxygenase activity
additional information
-
alkylating and oxidizing reagents convert oxygenase to oxidase; various sulfhydryl reagents including certain mercurials
-
additional information
-
at low lysine concentrations, inhibition by a variety of buffers
-
additional information
-
alkylating and oxidizing reagents convert oxygenase to oxidase
-
additional information
4-chloromercuribenzoate inhibits only the oxidase activity of the bifunctional enzyme, while the monooxygenase activity is not affected
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
increases oxidase and dehydrogenase activities, maximal rate of oxidation of lysine at 4-5 mol p-chloromercuribenzoate per mol enzyme, for arginine at 3 mol per mol enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.018
phenazine methosulfate
-
dehydrogenation of alanine and propylamine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.108
purified recombinant enzyme, pH 7,0, 30°C, substrate L-arginine
0.146
purified recombinant enzyme, pH 7,0, 30°C, substrate L-ornithine
0.532
purified recombinant enzyme, pH 7,0, 30°C, substrate L-lysine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.5
9.5
-
L-ornithine oxidase activity and L-lysine monooxygenase activity